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AGGF1 encodes an angiogenic factor that promotes proliferation of endothelial cells. Additionally we are shipping AGGF1 Antibodies (91) and AGGF1 Kits (27) and many more products for this protein.
Showing 7 out of 8 products:
Bmp-induced activation of beta-catenin (show CTNNB1 Proteins) through Aggf1 regulates caudal vein development by promoting the Nr2f2 (show NR2F2 Proteins)-dependent differentiation of venous endothelial cells and their survival.
aggf1 is involved in differentiation of both hematopoietic and endothelial lineages and acts upstream of scl (show TAL1 Proteins), fli1 (show FLI1 Proteins), and etsrp (show ETV2 Proteins) in specification of hemangioblasts
Our study establishes AGGF1 as an angiogenic factor (show VEGFA Proteins) with an important role in the specification of vein identity and suggests that AGGF1-mediated AKT (show AKT1 Proteins) signaling is responsible for establishing venous cell fate
Aggf1 has a role in regulating vascular injury.
High expression of AGGF1 predicts poor prognosis in gastric cancer patients.
AGGF1 gene polymorphism does not affect the risk of varicose veins of the legs in ethnic Russians.
Overexpression of AGGF1 is correlated with angiogenesis in hepatocellular carcinoma.
AGGF1 reduces myocardial apoptosis and inflammation and enhances angiogenesis, leading to decreased infarct size after I/R injury.
results of this study indicate that hypoxia down-regulates expression of the AGGF1 protein, but not AGGF1 mRNA, by inducing expression of miR (show MLXIP Proteins)-27a
AGGF1 potently attenuated TNF-alpha (show TNF Proteins) triggered NF-kappaB (show NFKB1 Proteins) pathway, as indicated by the decreased promoter activity, nuclear distribution and phosphorylation of NF-kappaB (show NFKB1 Proteins) p65 (show GORASP1 Proteins) subunit as well as the increased protein level of IkappaBalpha (show NFKBIA Proteins).
analysis of sphingolipid modulation of angio (show VEGFA Proteins)genic factor expression in n (show ARHGEF16 Proteins)euroblastoma
results define VG5Q as an angiogenic factor (show VEGFA Proteins), establish VG5Q as a susceptibility gene for Klippel-Trenaunay syndrome, and show that increased angiogenesis is a molecular pathogenic mechanism of KTS
VG5Q, E133K is a mutation that causes Klippel-Trenaunay and other overgrowth syndromes.
Together with recent identification of somatic mutations in p110a (encoded by PIK3CA (show PIK3CA Proteins)), our data establish a potential mechanistic link between AGGF1 and PIK3CA (show PIK3CA Proteins), the two genes identified for Klippel-Trenaunay syndrome (KTS)
Data indicate that angiogenic factor (show VEGFA Proteins) Aggf1+/- knockout (KO) mice show reduced autophagy, which was associated with inhibition of angiogenesis and larger infarct areas.
Mechanistically, Aggf1 activated the expression of gluconeogenesis gene and skewed the insulin (show INS Proteins) signaling pathway to induce insulin (show INS Proteins) resistance. Taken together, our data suggest that Aggf1 plays a role in steatosis in vivo and as such may be a new target in the development of therapeutics solutions against steatosis.
Sphingolipid modulation of angiogenic factor (show VEGFA Proteins) expression in neuroblastoma (show ARHGEF16 Proteins)
This gene encodes an angiogenic factor that promotes proliferation of endothelial cells. Mutations in this gene are associated with a susceptibility to Klippel-Trenaunay syndrome. Pseudogenes of this gene are found on chromosomes 3, 4, 10 and 16.
angiogenic factor with G patch and FHA domains 1
, angiogenic factor VG5Q
, G patch domain-containing protein 7
, vasculogenesis gene on 5q protein